ID I4BV19_ACEMN Unreviewed; 401 AA. AC I4BV19; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 27-MAR-2024, entry version 60. DE RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118}; GN Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=Anamo_0198 {ECO:0000313|EMBL:AFM20866.1}, Anamo_0472 GN {ECO:0000313|EMBL:AFM21126.1}; OS Acetomicrobium mobile (strain ATCC BAA-54 / DSM 13181 / JCM 12221 / NGA) OS (Anaerobaculum mobile). OC Bacteria; Synergistota; Synergistia; Synergistales; Acetomicrobiaceae; OC Acetomicrobium. OX NCBI_TaxID=891968 {ECO:0000313|EMBL:AFM21126.1, ECO:0000313|Proteomes:UP000006061}; RN [1] {ECO:0000313|EMBL:AFM21126.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13181 {ECO:0000313|EMBL:AFM21126.1}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Held B., RA Kyrpides N., Mavromatis K., Ivanova N., Last F.I., Brettin T., Detter J.C., RA Han C., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of Anaerobaculum mobile DSM 13181."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000006061} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-54 / DSM 13181 / NGA RC {ECO:0000313|Proteomes:UP000006061}; RX PubMed=23961311; DOI=10.4056/sigs.3547050; RA Mavromatis K., Stackebrandt E., Held B., Lapidus A., Nolan M., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Mikhailova N., Huntemann M., Pati A., RA Chen A., Palaniappan K., Land M., Rohde M., Spring S., Goker M., Woyke T., RA Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of the moderate thermophile Anaerobaculum mobile RT type strain (NGA(T))."; RL Stand. Genomic Sci. 8:47-57(2013). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- CC tRNA to the A-site of ribosomes during protein biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00118}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A CC subfamily. {ECO:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP- CC Rule:MF_00118}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP003198; AFM20866.1; -; Genomic_DNA. DR EMBL; CP003198; AFM21126.1; -; Genomic_DNA. DR RefSeq; WP_014806106.1; NC_018024.1. DR AlphaFoldDB; I4BV19; -. DR STRING; 891968.Anamo_0198; -. DR KEGG; amo:Anamo_0198; -. DR KEGG; amo:Anamo_0472; -. DR PATRIC; fig|891968.3.peg.201; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_0; -. DR Proteomes; UP000006061; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule. DR CDD; cd01884; EF_Tu; 1. DR CDD; cd03697; EFTU_II; 1. DR CDD; cd03707; EFTU_III; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. DR HAMAP; MF_00118_B; EF_Tu_B; 1. DR InterPro; IPR041709; EF-Tu_GTP-bd. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR033720; EFTU_2. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR NCBIfam; TIGR00485; EF-Tu; 1. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1. DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}; KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP- KW Rule:MF_00118}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00118}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00118}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00118}; Reference proteome {ECO:0000313|Proteomes:UP000006061}. FT DOMAIN 10..212 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT BINDING 19..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 81..85 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 136..139 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 401 AA; 44329 MW; D656F6C444B34666 CRC64; MAKSKFERVK PHLNIGTIGH IDHGKTTLTA AITRVLSTAG FADFTPFDQI DKAPEERERG ITISISHVEY QTEHRHYAHI DCPGHADYIK NMITGAAQMD GAILVVSAAD GPMPQTREHV LLARQVNVPV IVVFMNKVDM VDDEELLDLV EMEVRELLSS YGFPGDEVPV IRGSALKALE CGCGKRDCPW CGKIWELMDA CDSYIPLPER PVDQPFLMPI EDVFSITGRG TVVTGRVERG RITPGEEVEI VGMREDKIKT VATSLEMFRK VLDEAIAGDN IGILLRGVDK EDVERGQVVA KPGTITPHKH FKAEIYVLKK EEGGRHTPFF NGYKPQFYFR TTDVTGEITL PEGVEMVMPG DNANIEVKLI VPVALEKGLR FAIREGGRTV GAGVVTDILD K //